4b36

Crystal Structure of Human Angiogenin with an Engineered Loop Exhibits Conformational Flexibility at the Functional Regions of the Molecule

Method: X-RAY DIFFRACTION Dmax: 84.1 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

ANGIOGENIN, EOSINOPHIL CATIONIC-RELATED PROTEIN

HOMO SAPIENS

UniProt P03950

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 25–107 Chain A; UniProt 116–147 Fragment:RESIDUES 25-107,111-120,116-147 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:1.75-2.5 M NACL Resolution 1.76 Å R-free 0.285
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 25–107 Chain B; UniProt 116–147 Fragment:RESIDUES 25-107,111-120,116-147 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:1.75-2.5 M NACL Resolution 1.76 Å R-free 0.285

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

53 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANGI_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–84; UniProt 25–107 Author chain A; PDBConstruct 95–126; UniProt 116–147 Author chain B; PDBConstruct 2–84; UniProt 25–107 Author chain B; PDBConstruct 95–126; UniProt 116–147

ANGIOGENIN, EOSINOPHIL CATIONIC-RELATED PROTEIN

HOMO SAPIENS

UniProt Q12762

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 111–120 Fragment:RESIDUES 25-107,111-120,116-147 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:1.75-2.5 M NACL Resolution 1.76 Å R-free 0.285
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 111–120 Fragment:RESIDUES 25-107,111-120,116-147 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:1.75-2.5 M NACL Resolution 1.76 Å R-free 0.285

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q12762_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 85–94; UniProt 111–120 Author chain B; PDBConstruct 85–94; UniProt 111–120

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 4b36

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4b36
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4b36
Deposition date deposition_date2012-07-20
Structure title titleCrystal Structure of Human Angiogenin with an Engineered Loop Exhibits Conformational Flexibility at the Functional Regions of the Molecule
Keywords keywordsHYDROLASE, EDN, ANG, ANTIVIRAL, ANGIOGENESIS, TUMOR, AMYOTROPHIC LATERAL SCLEROSIS, PARKINSONS DISEASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier23.11
Radius of gyration Rg (electron density) rg_electron22.64
Forward intensity I(0) i013642100.00
Molecular weight molecular_weight26057.0 kDa
Excluded volume excluded_volume31929 ų
Envelope volume envelope_volume40746 ų
Hydration-shell volume shell_volume16410 ų
Envelope diameter envelope_diameter87.3
Shell Rg shell_rg27.05
Envelope Rg envelope_rg22.97
Shape Rg shape_rg22.62
Total Rg total_rg23.27
Total atoms total_atoms1822
Residues n_residues229
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax84.1
Rg (real space) rg_real23.35
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.3640e+07
I(0) uncertainty (real space) i0_real_error2.0150e+05
Rg (reciprocal space) rg_reciprocal23.29
I(0) (reciprocal space) i0_reciprocal13640000.0000
Solution quality estimate total_estimate0.8016
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.548
Kurtosis Kurtosis kurtosis-0.239
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3825000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.646; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.495; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4b36a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.5 — RNase A-like
Superfamily Superfamily superfamilyd.5.1 — RNase A-like
Family Family familyd.5.1.1 — Ribonuclease A-like
Domain ID domain_idd4b36b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.5 — RNase A-like
Superfamily Superfamily superfamilyd.5.1 — RNase A-like
Family Family familyd.5.1.1 — Ribonuclease A-like

CATH v4.4 (2 domains)

Domain ID domain_id4b36A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain
Domain ID domain_id4b36B00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain

8. Citations (1)

9. Files and Curves (10)